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dc.contributor.authorQuesada, Orestes
dc.contributor.authorGonzález-Freire, Carol
dc.contributor.authorColón-Sáez, José O.
dc.contributor.authorFernández-García, Emily
dc.contributor.authorMercado, Juan
dc.contributor.authorDávila, Alejandro
dc.contributor.authorMorales, Reginald
dc.contributor.authorLasalde-Dominicci, José A.
dc.date.accessioned2017-03-23T22:25:51Z
dc.date.available2017-03-23T22:25:51Z
dc.date.copyrightOpen — authors articles are freely available to all and as the author, authors retain copyright.en_USA
dc.date.issued2016-09-19
dc.identifier.citationQuesada, Orestes et al. “Uncovering the Lipidic Basis for the Preparation of Functional Nicotinic Acetylcholine Receptor Detergent Complexes for Structural Studies.” Scientific Reports 6 (2016): 32766. doi:10.1038/srep32766.en_US
dc.identifier.issn2045-2322
dc.identifier.urihttp://hdl.handle.net/11721/1571
dc.description.abstractThis study compares the lipid composition, including individual phospholipid molecular species of solubilized nAChR detergent complexes (nAChR-DCs) with those of the bulk lipids from their source, Torpedo californica (Tc) electric tissue. This lipidomic analysis revealed seventy-seven (77) phospholipid species in the Tc tissue. Analysis of affinity-purified nAChR-DCs prepared with C-12 to C-16 phospholipid analog detergents alkylphosphocholine (FC) and lysofoscholine (LFC) demonstrated that nAChRDCs prepared with FC12, LFC14, and LFC16 contained >60 phospholipids/nAChR, which was more than twice of those prepared with FC14, FC16, and LFC12. Significantly, all the nAChR-DCs lacked ethanolamine and anionic phospholipids, contained only four cholesterol molecules, and a limited number of phospholipid molecular species per nAChR. Upon incorporation into oocytes, FC12 produce significant functionality, whereas LFC14 and LFC16 nAChR-DCs displayed an increased functionality as compared to the crude Tc membrane. All three nAChR-DCs displayed different degrees of alterations in macroscopic activation and desensitization kinetics.en_US
dc.description.sponsorshipThis work was supported by the National Institutes of Health (NIH) Grants; 1R01GM098343 (JALD and OQ), Neuroimaging and Electrophysiology Facility Grant NIH P20 GM 103642 (JALD and OQ), Minority Access to Research Careers; (MARC) 5T34GM07821 (RM and OQ) and Research Initiative for Scientific Enhancement (RISE) 5R25GM061151 (RM and OQ) University of Puerto Rico Río Piedras Campus Institutional Funds for Research (JALD and OQ).en_USA
dc.Format.extent710.74 KBen_USA
dc.language.isoen_USen_US
dc.publisherNature / Scientific Reportsen_US
dc.titleUncovering the lipidic basis for the preparation of functional nicotinic acetylcholine receptor detergent complexes for structural studies.en_US
dc.typeArticleen_US
dc.rights.licenceCC BY license (Creative Commons Attribution 4.0 International License). All papers are available to the entire scientific community immediately after publication, with no barriers to access.en_USA
dcterms.licenseCC BY license (Creative Commons Attribution 4.0 International License). All papers are available to the entire scientific community immediately after publication, with no barriers to access.en_USA
dcterms.rightsOpen — authors articles are freely available to all and as the author, authors retain copyright.en_USA
dcterms.rightsHolderOpen — authors articles are freely available to all and as the author, authors retain copyright.en_USA
dc.description.doi10.1038/srep32766en_USA
dc.local.DepartmentDepartment of Biologyen_USA
dc.local.FacultyCollege of Natural Sciencesen_USA
dc.contributor.campusUniversity of Puerto Rico, Río Piedras Campus


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CC BY license (Creative Commons Attribution 4.0 International License). All papers are available to the entire scientific community immediately after publication, with no barriers to access.
Except where otherwise noted, this item's license is described as CC BY license (Creative Commons Attribution 4.0 International License). All papers are available to the entire scientific community immediately after publication, with no barriers to access.